Cold and thermal neutron scattering in liquid water—II: Scattering laws and group constants for HO and DO

Edura, Yoshinobu; Morishima, N.

doi:10.1016/j.nima.2005.01.302

Cited by 5 publications

(7 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Fitting of the water diffusion in the D 2 O-buffer measured on IN5 yields the values 103.1 and 157.2 Å 2 /ns at 5 and 22 • C, respectively (see Appendix A for details). The measured values are close to the literature values of 104.7 and 159.6 Å 2 /ns at 5 and 22 • C, 21,22 respectively. Thereby, the whole series of data treatment procedures from binning, subtraction, resolution modelling to fitting the Fourier transforms is validated.…”

Section: B Inelastic Scatteringsupporting

confidence: 89%

“…Solid symbols: T = 5 • C, open symbols: T = 22 • C.The high temperature data can be scaled to match the low temperature values by the division factor 1.5. In the covered low Q-regime, simple constant diffusion with values that match the literature values21,22 is observed.of the reference vanadium spectra. The resolution function can be written in terms of Fourier transforms,R(Q,ω) = N  i=1  a i e −(w i t) 2 /4 2π 3/2 w i cos([ω − ω i ] t)dt,(B2) the components of this Gaussian representations decay fast in the time domain enabling an efficient and accurate numerical Fourier-transform integration of the intermediate structure factor S(Q,t) over a finite time domain, I(Q,ω)…”

supporting

confidence: 82%

See 1 more Smart Citation

Fast internal dynamics in alcohol dehydrogenase

Monkenbusch

Stadler

Biehl

et al. 2015

The Journal of Chemical Physics

View full text Add to dashboard Cite

Large-scale domain motions in alcohol dehydrogenase (ADH) have been observed previously by neutron spin-echo spectroscopy (NSE). We have extended the investigation on the dynamics of ADH in solution by using high-resolution neutron time-of-flight (TOF) and neutron backscattering (BS) spectroscopy in the incoherent scattering range. The observed hydrogen dynamics were interpreted in terms of three mobility classes, which allowed a simultaneous description of the measured TOF and BS spectra. In addition to the slow global protein diffusion and domain motions observed by NSE, a fast internal process could be identified. Around one third of the protons in ADH participate in the fast localized diffusive motion. The diffusion coefficient of the fast internal motions is around two third of the value of the surrounding D2O solvent. It is tempting to associate the fast internal process with solvent exposed amino acid residues with dangling side chains.

show abstract

Section: B Inelastic Scatteringsupporting

confidence: 89%

supporting

confidence: 82%

Fast internal dynamics in alcohol dehydrogenase

Monkenbusch

Stadler

Biehl

et al. 2015

The Journal of Chemical Physics

View full text Add to dashboard Cite

show abstract

“…The residence times of H 2 O and D 2 O are reported to have similar values. 44 The observed type of motions on the picosecond time-scale has been attributed to rotational and librational motions of amino acid side-chains along the C-C bonds. 45 More recently, we have attributed the observed dynamics to the jumps of aminoacid side-chains mostly located on the surface of the protein.…”

Section: Internal Protein Diffusive Motionsmentioning

confidence: 99%

“…6(C). The diffusion coefficients of H 2 O and D 2 O bulk solvents 43,44 are also plotted in Fig. 6(B) and the residence times of H 2 O/D 2 O in Fig.…”

Section: Internal Protein Diffusive Motionsmentioning

confidence: 99%

“…The diffusivity of internal protein motions on the picosecond time-scale agrees well with the values of H 2 O bulk solvent. The diffusion coefficients of D 2 O buffer, which was used as solvent for the neutron scattering experiments, are significantly lower than those of internal protein 44 The dashed line in (B) are diffusion coefficients of H 2 O solvent. 43 dynamics.…”

Section: Internal Protein Diffusive Motionsmentioning

confidence: 99%

See 1 more Smart Citation

Picosecond to nanosecond dynamics provide a source of conformational entropy for protein folding

Stadler

Demmel

Ollivier

et al. 2016

Phys. Chem. Chem. Phys.

View full text Add to dashboard Cite

Myoglobin can be trapped in fully folded structures, partially folded molten globules, and unfolded states under stable equilibrium conditions. Here, we report an experimental study on the conformational dynamics of different folded conformational states of apo- and holomyoglobin in solution. Global protein diffusion and internal molecular motions were probed by neutron time-of-flight and neutron backscattering spectroscopy on the picosecond and nanosecond time scales. Global protein diffusion was found to depend on the α-helical content of the protein suggesting that charges on the macromolecule increase the short-time diffusion of protein. With regard to the molten globules, a gel-like phase due to protein entanglement and interactions with neighbouring macromolecules was visible due to a reduction of the global diffusion coefficients on the nanosecond time scale. Diffusion coefficients, residence and relaxation times of internal protein dynamics and root mean square displacements of localised internal motions were determined for the investigated structural states. The difference in conformational entropy ΔSconf of the protein between the unfolded and the partially or fully folded conformations was extracted from the measured root mean square displacements. Using thermodynamic parameters from the literature and the experimentally determined ΔSconf values we could identify the entropic contribution of the hydration shell ΔShydr of the different folded states. Our results point out the relevance of conformational entropy of the protein and the hydration shell for stability and folding of myoglobin.

show abstract